Laccase (EC 1.10.3.2) is an enzyme belonging to the polyphenol oxidase groups, which plays an important role in the oxidation of a wide variety of aromatic substrates, such as lignin, phenols, polyamines, and aryl diamines, as well as a number of other phenolic compounds or inorganic ions in the presence of oxygen. Laccase is widely applied in many fields, especially in the textile industry, dyeing, and environmental pollution treatment. In this study, we have successfully cloned and expressed cDNA coding for laccase from Pleurotus pulmonarius MPN18 (PpLac). cDNA corresponds to the gene laccase (1566 bp) that was inserted into pET 21a(+) vector and expressed in E. coli BL21, and the recombinant enzyme was purified through HisTrapTM sp 5mL column. The purified PpLac had an activity of 899.8 U, a 74% yield with a purity of 15.2 -fold, and was checked by SDS-PAGE with a molecular weight of Mw = 55 kDa. The enzyme displayed optimal activity at 50 ºC, pH = 4.0. It had an optimal activity of 20-40 ºC after 120 min incubation and pH = 4.0 after the incubation in 6 h. In the future, the recombinant enzyme will be characterized for supplementation into an enzyme cocktail for the treatment of lignocellulosic material.